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Results for “Glyceric Acids”

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At least 649 records · Page 36Linked to original sources
PubMed1996

Reconstitution of the hexose phosphate translocator from the envelope membranes of wheat endosperm amyloplasts.

Amyloplasts were isolated and purified from wheat endosperm and the envelope membranes reconstituted into liposomes. Envelope membranes were solubilized in n-octyl beta-D-glucopyranoside and mixed with liposomes supplemented with 5.6 mol% cholesterol to produce proteoliposomes of defined size, which showed negligible leakage of internal substrates. Transport experiments with proteoliposomes revealed a counter-exchange of glucose 1-phosphate (Glc1P), glucose 6-phosphate (Glc6P), inorganic phosphate (Pi), 3-phosphoglycerate and dihydroxyacetone phosphate. The Glc1P/Pi counter-exchange reaction exhibited an apparent K(m) for Glc1P of 0.4 mM. Glc6P was a competitive inhibitor of Glc1P transport (Ki 0.8 mM), and the two hexose phosphates could exchange with each other, indicating the operation of a single carrier protein. Glc1P/Pi antiport in proteoliposomes showed an exchange stoichiometry at pH 8.0 of 1 mol of phosphate transported per mol of sugar phosphate.

Cell Membrane↗
PubMed1968

Molecular diagnosis.

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Alcohol Oxidoreductases↗
PubMed1999

Glycolytic enzyme activity in hypotonically treated boar spermatozoa.

Treatment of washed boar sperm with hypotonic phosphate buffer disrupted the cytoplasmic membrane and released the soluble contents and phosphofructokinase, but the other glycolytic enzymes and lactate dehydrogenase were retained. Addition of the appropriate substrates and co-factor(s) to preparations of treated cells in phosphate-buffered saline showed that enzyme activity could be re-instated. This simple preparation should be of assistance in the investigation of specific sections of the glycolytic pathway without the use of chemical inhibitors.

Adenosine Diphosphate↗
PubMed1972

Functional nonequivalence of and hemes in human adult hemoglobin.

Nuclear magnetic resonance studies of the contact-shifted spectra of heme protons in deoxyhemoglobin A from human adults show conclusively that oxygen binds to the alpha hemes in preference to the beta hemes. The preferential binding is produced in 10% hemoglobin solution at neutral pH by either a 15-fold molar excess of 2,3-diphosphoglycerate or a 5-fold molar excess of inositol hexaphosphate. Preferential binding is not observable in the absence of the organic phosphates. The results indicate that the oxygenation of hemoglobin may be described by a sequential model, or by a concerted model that allows the alpha hemes to bind ligand first.

Adult↗
PubMed1973

Can a non-Mendelian mutation affect both chloroplast and mithchondrial ribosomes?

Chloroplast ribosomes isolated from a spectinomycin-resistant mutant (spr-1-27-3) of Chlamydomonas reinhardtii that displays non-Mendelian inheritance fail to bind labeled antibiotic, in contrast to ribosomes from wild-type cells. In vitro resistance of this mutant appears to result from the absence of a specific protein in the small subunit of the chloroplast ribosome. However, chloroplast protein synthesis in the mutant and wild type shows identical sensitivity to spectinomycin in short-term in vivo experiments where ribulosediphosphate carboxylase serves as the marker. Long-term experiments demonstrate that the mutant can grow in the presence of spectinomycin only when acetate is supplied as a carbon source. Mitochondrial structure and function of the mutant are not affected by the antibiotic, whereas chloroplast structure and function are. Apparently, the mitochondrion, rather than the chloroplast, of this mutant is resistant to spectinomycin in vivo. We hypothesize that the gene product of the spr locus is a protein common to both chloroplast and mitochondrial ribosomes. The mutant gene product, in vivo, confers resistance on mitochondrial, but not chloroplast, ribosomes. We suppose that the mutant spr protein loosely attaches to chloroplast ribosomes in vivo so that the antibiotic is bound and blocks protein synthesis, but it dissociates during isolation, resulting in loss of the binding site.

Binding Sites↗
PubMed1987

3-Phosphoglycerate-dependent protein phosphorylation.

The importance of protein phosphorylation in biological regulation is widely recognized; thus, a number of extracellular signal- and second messenger-linked protein kinases have been well characterized, and various substrates for these kinases have been identified. We present evidence that the glycolytic intermediate 3-phosphoglycerate can cause a marked stimulation of phosphorylation of specific proteins in mammalian tissues. In the brain, there are at least two types of 3-phosphoglycerate-dependent protein phosphorylation systems, which differ in activator specificity, substrate specificity, and sensitivity to the activator. Both of these phosphorylation systems are, however, insensitive to cAMP, cGMP, Ca2+, calmodulin, and protein kinase C activators and have characteristics different from those of casein kinase II-catalyzed protein phosphorylation. The most prominent endogenous substrates in the bovine brain are rather minor proteins with minimal molecular masses of 72 and 155 kDa, which were not detected in "nonnervous" tissues such as heart, liver, lung, and kidney. In nonnervous tissues, 3-phosphoglycerate affected the state of phosphorylation of other proteins. Evidence provided suggests the occurrence of an as yet undescribed type of protein kinase, which may be designated 3-phosphoglycerate-dependent protein kinase, in mammalian tissues.

Animals↗